SE1L1_MOUSE
ID SE1L1_MOUSE Reviewed; 790 AA.
AC Q9Z2G6; Q9DBD8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein sel-1 homolog 1;
DE AltName: Full=Suppressor of lin-12-like protein 1;
DE Short=Sel-1L;
DE Flags: Precursor;
GN Name=Sel1l; Synonyms=Sel1h;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=9858735; DOI=10.1016/s0925-4773(98)00146-4;
RA Donoviel D.B., Donoviel M.S., Fan E., Hadjantonakis A.-K., Bernstein A.;
RT "Cloning and characterization of Sel-1l, a murine homolog of the C. elegans
RT sel-1 gene.";
RL Mech. Dev. 78:203-207(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MISCELLANEOUS.
RX PubMed=20170518; DOI=10.1186/1471-213x-10-19;
RA Li S., Francisco A.B., Munroe R.J., Schimenti J.C., Long Q.;
RT "SEL1L deficiency impairs growth and differentiation of pancreatic
RT epithelial cells.";
RL BMC Dev. Biol. 10:19-19(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, GLYCOSYLATION, AND
RP INTERACTION WITH SYVN1; LPL AND LMF1.
RX PubMed=25066055; DOI=10.1016/j.cmet.2014.06.015;
RA Sha H., Sun S., Francisco A.B., Ehrhardt N., Xue Z., Liu L., Lawrence P.,
RA Mattijssen F., Guber R.D., Panhwar M.S., Brenna J.T., Shi H., Xue B.,
RA Kersten S., Bensadoun A., Peterfy M., Long Q., Qi L.;
RT "The ER-associated degradation adaptor protein Sel1L regulates LPL
RT secretion and lipid metabolism.";
RL Cell Metab. 20:458-470(2014).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24453213; DOI=10.1073/pnas.1318114111;
RA Sun S., Shi G., Han X., Francisco A.B., Ji Y., Mendonca N., Liu X.,
RA Locasale J.W., Simpson K.W., Duhamel G.E., Kersten S., Yates J.R. III,
RA Long Q., Qi L.;
RT "Sel1L is indispensable for mammalian endoplasmic reticulum-associated
RT degradation, endoplasmic reticulum homeostasis, and survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E582-E591(2014).
RN [7] {ECO:0007744|PDB:5B26}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 348-533, SUBUNIT, INTERACTION
RP WITH SYVN1, REGION, AND MUTAGENESIS OF 512-GLY-GLY-513; 515-ILE-LEU-516;
RP TYR-519 AND LEU-521.
RX PubMed=27064360; DOI=10.1038/srep20261;
RA Jeong H., Sim H.J., Song E.K., Lee H., Ha S.C., Jun Y., Park T.J., Lee C.;
RT "Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD
RT pathway.";
RL Sci. Rep. 6:20261-20261(2016).
CC -!- FUNCTION: Plays a role in the endoplasmic reticulum quality control
CC (ERQC) system also called ER-associated degradation (ERAD) involved in
CC ubiquitin-dependent degradation of misfolded endoplasmic reticulum
CC proteins (PubMed:25066055, PubMed:24453213). Enhances SYVN1 stability
CC (PubMed:24453213). Plays a role in LPL maturation and secretion
CC (PubMed:25066055). Required for normal differentiation of the pancreas
CC epithelium, and for normal exocrine function and survival of pancreatic
CC cells (PubMed:20170518, PubMed:24453213). May play a role in Notch
CC signaling (PubMed:20170518). {ECO:0000269|PubMed:20170518,
CC ECO:0000269|PubMed:24453213, ECO:0000269|PubMed:25066055}.
CC -!- SUBUNIT: Homodimer and homooligomer (PubMed:27064360). May form a
CC complex with ERLEC1, HSPA5, OS9, and SYVN1 (By similarity). Interacts
CC with FOXRED2 and EDEM1 (By similarity). Interacts with LPL and LMF1;
CC may stabilize the complex formed by LPL and LMF1 and thereby promote
CC the export of LPL dimers (PubMed:25066055). Component of the HRD1
CC complex, which comprises at least SYNV1/HRD1, DERL1/2, FAM8A1,
CC HERPUD1/HERP, OS9, SEL1L and UBE2J1 (By similarity). SYNV1 assembles
CC with SEL1L and FAM8A1 through its transmembrane domains, but
CC interaction with its cytoplasmic domain is required to confer stability
CC to FAM8A1 and enhance recruitment of HERPUD1 (By similarity). The
CC interaction with SYNV1/HRD1 is direct (PubMed:25066055,
CC PubMed:27064360). {ECO:0000250|UniProtKB:Q9UBV2,
CC ECO:0000269|PubMed:25066055, ECO:0000269|PubMed:27064360}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UBV2}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9UBV2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z2G6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z2G6-2; Sequence=VSP_004384;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas, white adipose tissue,
CC liver and spleen (at protein level) (PubMed:25066055, PubMed:24453213).
CC Detected in heart, brain, spleen, lung, liver, kidney and testis
CC (PubMed:9858735). {ECO:0000269|PubMed:24453213,
CC ECO:0000269|PubMed:25066055, ECO:0000269|PubMed:9858735}.
CC -!- DEVELOPMENTAL STAGE: First detected at 12.5 dpc in a small number of
CC pancreas epithelial cells. Highly expressed in embryonic pancreas
CC epithelium at later stages of embryonic development.
CC {ECO:0000269|PubMed:20170518}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:25066055}.
CC -!- DISRUPTION PHENOTYPE: Taxomifen-inducible gene disruption in adult mice
CC leads to premature death within 3 weeks after the onset of taxomifen
CC treatment. Mice progressively loose weight and become moribund despite
CC increased food intake and normal blood glucose levels, suggesting
CC nutrient maladsorption. After eight days of treatment, the pancreas was
CC diffusely dark red and soft, suggesting severe pancreas atrophy. Still,
CC the endocrine parts of the pancreas were not affected. Pancreas weight
CC was about half of that of wild-type, the size of secretory zymogen
CC granules was reduced and pancreatic lipase and alpha-amylase levels
CC were strongly reduced. Besides, the morphology of the endoplasmic
CC reticulum in pancreas acinar cells was abnormal, with swollen and
CC fragmented cisternae. Likewise, SYVN1 protein levels are decreased,
CC while those of other ERAD markers are increased (PubMed:24453213).
CC Adipocyte-specific gene disruption does not give rise to any obvious
CC phenotype when mice are kept on a low-fat diet. Mutant mice are
CC resistant to diet-induced obesity when kept on a high-fat diet, in
CC spite of normal food intake and physical activity. Mutant mice show
CC dramatically reduced accumulation of fat mass relative to wild-type,
CC while lean mass is not affected. Intriguingly, mutant mice display
CC enlarged livers that develop steatosis and increased triglyceride
CC levels. Mutant mice display increased fasting serum triglyceride and
CC insulin levels. Likewise, mutant mice display hypertriglyceridemia
CC after feeding, especially on a high-fat diet. In spite of increased
CC cellular LPL levels, LPL secretion is reduced by 80 to 90%
CC (PubMed:25066055). {ECO:0000269|PubMed:24453213,
CC ECO:0000269|PubMed:25066055}.
CC -!- MISCELLANEOUS: Gene disruption after residue 465 and replacement of the
CC C-terminus with a beta-galactosidase-neomycin reporter gene construct
CC leads to complete embryonic lethality; most die before 13.5 dpc. Only
CC 5% of the embryos are viable at 15.5 dpc. Mutant embryos display
CC defects in the differentiation of the pancreas epithelium. The defects
CC in pancreas differentiation can be alleviated by pharmacological
CC inhibition of Notch signaling (in vitro).
CC {ECO:0000269|PubMed:20170518}.
CC -!- SIMILARITY: Belongs to the sel-1 family. {ECO:0000305}.
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DR EMBL; AF063095; AAD05210.1; -; mRNA.
DR EMBL; AK005023; BAB23750.1; -; mRNA.
DR CCDS; CCDS26091.1; -. [Q9Z2G6-1]
DR CCDS; CCDS49137.1; -. [Q9Z2G6-2]
DR RefSeq; NP_001034178.1; NM_001039089.1. [Q9Z2G6-1]
DR RefSeq; NP_035474.1; NM_011344.2. [Q9Z2G6-2]
DR PDB; 5B26; X-ray; 2.60 A; A/B/C/D=348-533.
DR PDBsum; 5B26; -.
DR AlphaFoldDB; Q9Z2G6; -.
DR SMR; Q9Z2G6; -.
DR BioGRID; 203153; 11.
DR DIP; DIP-61846N; -.
DR IntAct; Q9Z2G6; 6.
DR STRING; 10090.ENSMUSP00000021347; -.
DR GlyConnect; 2642; 5 N-Linked glycans (3 sites).
DR GlyGen; Q9Z2G6; 5 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; Q9Z2G6; -.
DR PhosphoSitePlus; Q9Z2G6; -.
DR EPD; Q9Z2G6; -.
DR jPOST; Q9Z2G6; -.
DR MaxQB; Q9Z2G6; -.
DR PaxDb; Q9Z2G6; -.
DR PRIDE; Q9Z2G6; -.
DR ProteomicsDB; 261142; -. [Q9Z2G6-1]
DR ProteomicsDB; 261143; -. [Q9Z2G6-2]
DR Antibodypedia; 13274; 272 antibodies from 30 providers.
DR Ensembl; ENSMUST00000021347; ENSMUSP00000021347; ENSMUSG00000020964. [Q9Z2G6-1]
DR Ensembl; ENSMUST00000167466; ENSMUSP00000129384; ENSMUSG00000020964. [Q9Z2G6-2]
DR GeneID; 20338; -.
DR KEGG; mmu:20338; -.
DR UCSC; uc007oky.1; mouse. [Q9Z2G6-1]
DR CTD; 6400; -.
DR MGI; MGI:1329016; Sel1l.
DR VEuPathDB; HostDB:ENSMUSG00000020964; -.
DR eggNOG; KOG1550; Eukaryota.
DR GeneTree; ENSGT00940000156671; -.
DR HOGENOM; CLU_007931_2_1_1; -.
DR InParanoid; Q9Z2G6; -.
DR OMA; DMLAKPR; -.
DR PhylomeDB; Q9Z2G6; -.
DR TreeFam; TF315257; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR BioGRID-ORCS; 20338; 16 hits in 73 CRISPR screens.
DR ChiTaRS; Sel1l; mouse.
DR PRO; PR:Q9Z2G6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9Z2G6; protein.
DR Bgee; ENSMUSG00000020964; Expressed in submandibular gland and 262 other tissues.
DR ExpressionAtlas; Q9Z2G6; baseline and differential.
DR Genevisible; Q9Z2G6; MM.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036503; P:ERAD pathway; IMP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:MGI.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:UniProtKB.
DR CDD; cd00062; FN2; 1.
DR Gene3D; 1.25.40.10; -; 3.
DR Gene3D; 2.10.10.10; -; 1.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF08238; Sel1; 12.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00671; SEL1; 11.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Notch signaling pathway; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..790
FT /note="Protein sel-1 homolog 1"
FT /id="PRO_0000022296"
FT TOPO_DOM 22..734
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 756..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 118..166
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT REPEAT 179..214
FT /note="Sel1-like 1"
FT REPEAT 215..250
FT /note="Sel1-like 2"
FT REPEAT 251..286
FT /note="Sel1-like 3"
FT REPEAT 287..322
FT /note="Sel1-like 4"
FT REPEAT 369..405
FT /note="Sel1-like 5"
FT REPEAT 406..442
FT /note="Sel1-like 6"
FT REPEAT 443..478
FT /note="Sel1-like 7"
FT REPEAT 479..514
FT /note="Sel1-like 8"
FT REPEAT 515..550
FT /note="Sel1-like 9"
FT REPEAT 623..658
FT /note="Sel1-like 10"
FT REPEAT 660..695
FT /note="Sel1-like 11"
FT REGION 22..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 23..733
FT /note="Interaction with ERLEC1, OS9 and SYVN1"
FT /evidence="ECO:0000250"
FT REGION 67..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..533
FT /note="Important for homodimerization and oligomerization"
FT /evidence="ECO:0000269|PubMed:27064360"
FT REGION 639..719
FT /note="Interaction with SYVN1"
FT /evidence="ECO:0000269|PubMed:27064360"
FT REGION 734..790
FT /note="Mediates retention in the endoplasmic reticulum"
FT /evidence="ECO:0000250"
FT REGION 763..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..790
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV2"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 137..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT VAR_SEQ 116..166
FT /note="GTAHGEPCHFPFLFLDKEYDECTSDGREDGRLWCATTYDYKTDEKWGFCET
FT -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9858735"
FT /id="VSP_004384"
FT MUTAGEN 512..513
FT /note="GG->KK: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:27064360"
FT MUTAGEN 515..516
FT /note="IL->AA: Abolishes homodimerization; when associated
FT with A-519."
FT /evidence="ECO:0000269|PubMed:27064360"
FT MUTAGEN 519
FT /note="Y->A: Abolishes homodimerization; when associated
FT with 515-A-A-516."
FT /evidence="ECO:0000269|PubMed:27064360"
FT MUTAGEN 521
FT /note="L->A: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:27064360"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:5B26"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:5B26"
FT HELIX 390..402
FT /evidence="ECO:0007829|PDB:5B26"
FT HELIX 406..417
FT /evidence="ECO:0007829|PDB:5B26"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:5B26"
FT HELIX 427..439
FT /evidence="ECO:0007829|PDB:5B26"
FT HELIX 443..454
FT /evidence="ECO:0007829|PDB:5B26"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:5B26"
FT HELIX 463..475
FT /evidence="ECO:0007829|PDB:5B26"
FT HELIX 479..490
FT /evidence="ECO:0007829|PDB:5B26"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:5B26"
FT HELIX 499..510
FT /evidence="ECO:0007829|PDB:5B26"
FT HELIX 517..521
FT /evidence="ECO:0007829|PDB:5B26"
SQ SEQUENCE 790 AA; 88340 MW; 47869F2AFB59B936 CRC64;
MQVRVRLSLL LLCAVLLGSA AATSDDKTNQ DDSLDSKSSL PTDESVKDHT TTGKVVAGQI
FVDSEEAEVE SLLQDEEDSS KTQEEEISFL ESPNPSSKTY EELKRVRKPV LTAIEGTAHG
EPCHFPFLFL DKEYDECTSD GREDGRLWCA TTYDYKTDEK WGFCETEEDA AKRRQMQEAE
MIYQAGMKIL NGSNRKSQKR EAYRYLQKAA GMNHTKALER VSYALLFGDY LTQNIQAAKE
MFEKLTEEGS PKGQTGLGFL YASGLGVNSS QAKALVYYTF GALGGNLIAH MILGYRYWAG
IGVLQSCESA LTHYRLVANH VASDISLTGG SVVQRIRLPD EVENPGMNSG MLEEDLIQYY
QFLAEKGDVQ AQVGLGQLHL HGGRGVEQNH QRAFDYFNLA ANAGNSHAMA FLGKMYSEGS
DIVPQSNETA LHYFKKAADM GNPVGQSGLG MAYLYGRGVQ VNYDLALKYF QKAAEQGWVD
GQLQLGSMYY NGIGVKRDYK QALKYFNLAS QGGHILAFYN LAQMHASGTG VMRSCHTAVE
LFKNVCERGR WSERLMTAYN SYKDEDYNAA VVQYLLLAEQ GYEVAQSNAA FILDQREATI
VGENETYPRA LLHWNRAASQ GYTVARIKLG DYHFYGFGTD VDYETAFIHY RLASEQQHSA
QAMFNLGYMH EKGLGIKQDI HLAKRFYDMA AEASPDAQVP VFLALCKLGV VYFLQYIREA
NIRDLFTQLD MDQLLGPEWD LYLMTIIALL LGTVIAYRQR QHQDIPVPRP PGPRPAPPQQ
EGPPEQQPPQ
